ID A0A452CA09_BALAS Unreviewed; 938 AA.
AC A0A452CA09;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Probable phospholipid-transporting ATPase IIB {ECO:0000313|RefSeq:XP_028019922.1};
GN Name=ATP9B {ECO:0000313|RefSeq:XP_028019922.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028019922.1};
RN [1] {ECO:0000313|RefSeq:XP_028019922.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028019922.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_028019922.1; XM_028164121.1.
DR AlphaFoldDB; A0A452CA09; -.
DR STRING; 310752.A0A452CA09; -.
DR InParanoid; A0A452CA09; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF50; PHOSPHOLIPID-TRANSPORTING ATPASE IIB-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..131
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 703..930
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 480..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 105623 MW; 7CCD76609FC54DCF CRC64;
MPLMMSEEGF ENDESDYHKL PRARIMRRKR GLEWFVCGGW KFLCTSCCDW LINICQRKRE
LKARTVWLGY PEKCEEKHPR NSIKNQKYNV FTFIPGVLYE QFKFFLNLYF LVVSCSQFVP
ALKIGYLYTY WAPLGFVLAV TIMREATDEF RRFQRDKEVN SQLYSKLTVR GKVQVKSSDI
QVGDLIIVEK NQRIPSDMVF LRTSEKAGSC FIRTDQLDGE TDWKLRVAVS CTQRLPALGD
LFSINAYVYA QKPQLDIHSF EGTFTRRCSK STCTRCSWQQ KEGRCPGDKY LEDSDPPIHE
SLSIENTLWA STVVASGTVI GVVIYTGKET RSVMNTSNPK NKVGLLDLEL NQLTKTLFLA
LVALSVVMVT LQGFSGPWYR SLFRFLLLFS YIIPISLRVN LDMGKAAYGW MIMKDENISG
TVVRTSTIPE ELGRLVYLLT DKTGTLTRNE MVFKRLHLGT VSYGTDTMDE IQNHLVNSYS
QTQAQASGNN ASSAPPRKAQ SSAPKVRKSV SSRVHEAVKA VALCHNVTPV YEARGAAGET
EFAEADQDFS DDNRTYQASS PDEIWMLTGD KLETATCIAK SSHLVSRTQD THVFRPVTSR
GEAHLELNAF RRKHDCALVI SGDSLEVCLK YYEHEFVELA CQCPAVVCCR CAPTQKAHIV
KLLQQHTGRR TCAIGDGGND VSMIQAADCG IGIEGKEGRQ ASLAADFSVP QFKHIGRLLM
VHGRSSYKRS AALSQFVMHR GLVISTMQAV FSSVFYFASV PLYQGFLMVG YATVYTMFPV
FSLVLDQDVK PEMAMLYPEL YKDLTKGRSL SCKTFLVWVL ISIYQGGILM SGALVLFESE
FVHVVAISFT ALVLTELLMV ALTVRTWHWL MAVAELLSLG CYVASLAFLN KYFDLAFITT
VTFVWKVSAI TVVSCLPLYV LKYLKRKLSP PSYSKLSS
//